Relationship between the specificity of IgA proteases and serotypes in Haemophilus influenzae.
Haemophilus influenzae is one of five bacterial species known to produce IgA proteases, enzymes that specifically cleave the human IgA1 heavy chain. Strains of H. influenzae produce three distinct types of IgA proteases that cleave different peptide bonds within the IgA1 hinge region. Type 1 protease cleaves the prolyl-seryl bond at position 231-232; type 2 protease cleaves the prolyl-threonyl bond at position 235-236, the same bond attacked by Neisseria gonorrhoeae and Neisseria meningitidis type 2 proteases. Type 3 protease yields a unique double Fd cleavage pattern; the exact peptide bonds cleaved have not been determined. The type of protease produced correlates with the serotype, but not with the biotype, of the isolate; serotypes A, B, D, and F produce primarily type 1 protease, whereas serotypes C and E produce only type 2 enzyme. Each nontypable strain yields one of the three protease types. These data further extend our knowledge of the extreme specificity of the IgA proteases and suggest that IgA protease type may be useful in the taxonomy and epidemiology of H. influenzae.
D055598:Chemical Phenomena; D002621:Chemistry; D006193:Haemophilus influenzae / Q000145:classification / Q000201:enzymology*; D007070:Immunoglobulin A / Q000378:metabolism*; D007143:Immunoglobulin Heavy Chains / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D012697:Serine Endopeptidases; D012703:Serotyping; D013379:Substrate Specificity
D007070:Immunoglobulin A; D007143:Immunoglobulin Heavy Chains; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase